Cloning and Expression in Pseudomonas putida of Two of the Histidine Utilization Genes from Rhizobium fredii

1997 ◽  
Vol 34 (1) ◽  
pp. 55-60
Author(s):  
Robert R. Burke ◽  
Diana D. Heard ◽  
Anthony J. Nieuwkoop
Keyword(s):  
Pseudomonas Putida ◽  
Cloning And Expression ◽  
Rhizobium Fredii

scholarly journals Molecular cloning and expression of Rhizobium fredii USDA 193 nodulation genes: extension of host range for nodulation.

1986 ◽  
Vol 168 (3) ◽  
pp. 1087-1095 ◽  
Author(s):  
N Ramakrishnan ◽  
R K Prakash ◽  
S Shantharam ◽  
N M Duteau ◽  
A G Atherly
Keyword(s):  
Host Range ◽  
Molecular Cloning ◽  
Cloning And Expression ◽  
Nodulation Genes ◽  
Rhizobium Fredii

scholarly journals Cloning and Expression of pca Genes from Pseudomonas putida in Escherichia coli

Microbiology ◽  
1988 ◽  
Vol 134 (11) ◽  
pp. 2877-2887 ◽  
Author(s):  
E. J. Hughes ◽  
M. K. Shapiro ◽  
J. E. Houghton ◽  
L. N. Ornston
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Putida ◽  
Cloning And Expression

Cloning and expression of a trehalose synthase from Pseudomonas putida KT2440 for the scale-up production of trehalose from maltose

2014 ◽  
Vol 60 (9) ◽  
pp. 599-604 ◽  
Author(s):  
Tengfei Wang ◽  
Shiru Jia ◽  
Kun Dai ◽  
Hongjuan Liu ◽  
Ruiming Wang
Keyword(s):  
Escherichia Coli ◽  
High Pressure ◽  
Pseudomonas Putida ◽  
Scale Up ◽  
Activity Analysis ◽  
Cloning And Expression ◽  
Pseudomonas Putida Kt2440 ◽  
Trehalose Synthase ◽  
E Coli ◽  
Optimal Activity

Trehalose synthase (TreS) is considered to be a potential biocatalyst for trehalose production. We aimed to scale-up produce the TreS protein in Escherichia coli and further investigate the bioconversion capacity of TreS. The treS gene from Pseudomonas putida KT2440 was amplified and expressed in E. coli BL21 (DE3). The recombinant TreS showed a molecular mass of 67 kDa. Activity analysis suggested that TreS had optimal activity at a temperature of 55 °C, a pH of 7.4, with a substrate concentration of 30%. High-pressure liquid chromatography results indicated that this enzyme had the ability to catalyze 59% maltose into trehalose, with about 5.1% glucose as by-product. Purification analysis showed that trehalose crystals with a purity of 98% were obtained by cooling trehalose solution. The TreS from P. putida KT2440 might be a candidate for trehalose production. Further study is needed to improve the trehalose conversion rate.

Cloning and expression of a Bacillus α-glucosidase gene in Escherichia coli, Zymomonas mobilis and Pseudomonas putida

1993 ◽  
Vol 29 (1-2) ◽  
pp. 189-203 ◽  
Author(s):  
Aneta T. Strzelecki ◽  
Amanda E. Goodman ◽  
Peter L. Rogers ◽  
John M. Watson
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Putida ◽  
Zymomonas Mobilis ◽  
Cloning And Expression
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